3U2Q: EF-Tu

EF-Tu (Escherichia coli) in complex with NVP-LFF571. Determined by X-ray diffraction at 2.7 Å resolution. Released 2 May 2012.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: Escherichia coli
Chains: 2
Atoms: 3,176
Mol. weight: 45.34 kDa
Ligands: MG, GDP
Released: 2 May 2012

Explore 3U2Q in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3U2Q contains 14 α-helices and 29 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 14 helices, 29 β-strands

Element	Residues	Length	Sheet
β-strand	11-15	5	1
β-strand	16-17	2	2
α-helix	24-39	16
α-helix	46-48	3
β-strand	65-71	7	1
β-strand	74-80	7	1
α-helix	84-93	10
β-strand	101-106	6	2
α-helix	113-125	13
β-strand	130-135	6	2
α-helix	148-159	12
β-strand	169-171	3	2
α-helix	176-179	4
α-helix	182-198	17
α-helix	200-204	5
α-helix	205-207	3
α-helix	209-210	2
β-strand	211-213	3	3
β-strand	217-220	4	4
β-strand	224-230	7	4
β-strand	233	1	3
β-strand	235-237	3	5
β-strand	241-246	6	3
β-strand	248-254	7	3
β-strand	255-260	6	4
β-strand	263-265	3	4
β-strand	267-269	3	5
β-strand	273-279	7	4
α-helix	283-285	3
β-strand	288	1	6
β-strand	290	1	6
β-strand	291-293	3	3
β-strand	299-310	12	7
α-helix	311-312	2
α-helix	313-315	3
β-strand	322-323	2	8
β-strand	329-332	4	7
β-strand	335-342	8	7
α-helix	343-344	2
β-strand	349-350	2	8
β-strand	355-368	14	7
β-strand	373-378	6	7
β-strand	381-391	11	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Elongation factor Tu 1	A	protein	394	Escherichia coli	P0CE47 (AlphaFold model)
Thiocillin GE2270 analogue NVP-LFF571	B	protein	12		Q7M0J8

Sequence of entity 1 (A), FASTA

>3U2Q_1 Elongation factor Tu 1 (chains A)
MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARG
ITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHI
LLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALE
GDAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVG
EEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIK
PHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMV
VTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLG

Sequence of entity 2 (B), FASTA

>3U2Q_2 Thiocillin GE2270 analogue NVP-LFF571 (chains B)
SCNCVCGFCCSX

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	1
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	1

Primary citation

Discovery of LFF571: an investigational agent for Clostridium difficile infection. LaMarche, M.J., Leeds, J.A., Amaral, A. et al. J Med Chem (2012) 55:2376-2387. DOI 10.1021/jm201685h · PubMed

Other PDB entries of the same protein (UniProt P0CE47 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9TBU 1.23 Å, E. coli EF-Tu-T62A:GDP AMPylated at T65
4PC3 1.83 Å, Elongation factor Tu:Ts complex with partially bound GDP
5JBQ 2.01 Å, Ef-tu (escherichia coli) in complex with thiomuracin analog
1EFC 2.05 Å, Intact elongation factor from e.coli
2HCJ 2.12 Å, Trypsin-modified Elongation Factor Tu in complex with tetracycline
3U6B 2.12 Å, Ef-tu (escherichia coli) in complex with nvp-ldi028
4P3Y 2.15 Å, Crystal structure of Acinetobacter baumannii DsbA in complex with EF-Tu
5MI8 2.18 Å, Structure of the phosphomimetic mutant of EF-Tu T383E
8FR3 2.23 Å, E. coli EF-Tu in complex with KKL-55
4G5G 2.3 Å, ef-tu (Escherichia coli) complexed with nvp-ldu796
1D8T 2.35 Å, Crystal structure of elongation factor, tu (ef-tu-mggdp) complexed with GE2270A, a…
5I4Q 2.35 Å, Contact-dependent inhibition system from Escherichia coli NC101 - ternary…

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